EC Number   |
Application |
Reference |
|---|
   2.4.1.41 | analysis |
development of a bump-hole chemical reporter system for studying GalNAc-T activity in vitro. GalNAc-T2 ire rationally engineered to contain an enlarged active site (hole) and probed with a collection of 20 (bumped) uridine diphosphate N-acetylgalactosamine analogs to identify enzyme-substrate pairs that retain peptide specificities but are otherwise completely orthogonal to native enzyme-substrate pairs. The approach is applicable to multiple GalNAc-T isoenzymes, including GalNAc-T1 and -T2 that prefer nonglycosylated peptide substrates and GalNAcT-10 that prefers a preglycosylated peptide substrate |
757070 |
| 2.4.1.41 | analysis |
development of isogenic cell-model systems withTet-On inducible expression of GalNAc-T genes GALNT2 and GALNT11 in a knockout background in HEK-293 cells to identify O-glycopeptides differentially affected by induction of GalNAc-T2 or -T11 |
757207 |
| 2.4.1.41 | drug development |
further studies of the substrate specificity of these and potentially additional enzymes are required, but it may be anticipated that this understanding will be significant for insight into O-glycosylation processing and of practical use, for example, for designing appropriate mammalian expression systems for recombinant glycoproteins in drug use |
659127 |
| 2.4.1.41 | drug development |
further studies of the substrate specificity of these and potentially additional enzymes are required, but it may be anticipated that this understanding will be significant for our insight into O-glycosylation processing and of practical use, for example, for designing appropriate mammalian expression systems for recombinant glycoproteins in drug use |
659127 |
| 2.4.1.41 | medicine |
cancer cells compared to normal cells exhibit altered glycosyltransferase activities, enzyme is a new tool for the investigation of motif peptide O-glycosylation alterations in pathological situations |
489192 |
| 2.4.1.41 | medicine |
isoform GalNAc-T1 is largely required for the Ebola virus surface glycoprotein-mediated adhesion defects. Despite its profound effect on surface glycoprotein function, the absence of GalNAc-T1 only modestly reduces the O-glycan mass of surface glycoprotein. A small segment of the mucin-like domain of the surface glycoprotein is critical for function and mutation of five glycan acceptor sites within this segment are sufficient to abrogate surface glycoprotein function |
757208 |
| 2.4.1.41 | medicine |
isoform GalNAc-T3 expression is an indicator of tumor differentiation in thyroid carcinoma |
737277 |
| 2.4.1.41 | medicine |
isoform GalNAc-T4 shows a stage-dependent expression at the different stages of colorectal cancer in 62 pair-matched tumor/normal tissues. GalNAc-T4 expression is significantly induced at stage I and II but not at stage III and IV. Overexpression of GalNAc-T4 in colorectal cancer cells enhances colony formation and sphere formation. Knockdown of GalNAc-T4 in colorectal cancer cells increases the cell migration and invasion, and leads to an epithelial-mesenchymal transition-like transition. Loss of GalNAc-T4 contributes to the dedifferentiation of colorectal cancer cells and high expression of GalNAc-T4 correlates to a good prognosis of patients |
756704 |
| 2.4.1.41 | medicine |
isoform GALNT3 expression significantly correlates with shorter progression-free survival intervals in epithelial ovarian cancer patients with advanced disease |
736918 |
| 2.4.1.41 | medicine |
isoform Galnt3-deficient mice serve as a model for the disease hyperphosphatemic familial tumoral calcinosis |
757237 |
